Biology, Pages 82-91 |
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Page 75
... are located , where ionic bonds can form , and so on . However , in the
crowded environment inside a cell , correct folding may be more of a problem
than it is in a test tube . The Protein - Folding Problem Biochemists now know the
amino 75.
... are located , where ionic bonds can form , and so on . However , in the
crowded environment inside a cell , correct folding may be more of a problem
than it is in a test tube . The Protein - Folding Problem Biochemists now know the
amino 75.
Page 77
Researchers have also discovered chaperonins ( also called chaperone proteins
) , protein molecules that assist the proper folding of other proteins ( Figure 5.23 )
. Chaperonins do not actually specify the correct final structure of a polypeptide ...
Researchers have also discovered chaperonins ( also called chaperone proteins
) , protein molecules that assist the proper folding of other proteins ( Figure 5.23 )
. Chaperonins do not actually specify the correct final structure of a polypeptide ...
Page 118
Which of the following could amylase break down ? ( Choose all that apply . )
cellulose b . chitin c . glycogen d . starch amylopectin a . e . 4. Choose the pair of
terms that correctly completes this sentence : as Nucleotides are to are to
proteins ...
Which of the following could amylase break down ? ( Choose all that apply . )
cellulose b . chitin c . glycogen d . starch amylopectin a . e . 4. Choose the pair of
terms that correctly completes this sentence : as Nucleotides are to are to
proteins ...
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Activity amino acid sequence answers arrangement atoms bind Biology blood bonds break build built called Carbohydrates carbon cell chaperonin chemical Chemistry complementary complex components compounds Concept conformation connected consists correct cytoplasm cytosine denatured denatured protein deoxyribose sugars determines differ directions DNA and Proteins DNA double helix DNA molecule Emergent endorphins environment enzyme evolutionary fats fatty acids Figure flow folding four function genes genetic information glucose glycosidic linkages hemoglobin humans hydrogen bonds interactions joined known linked macromolecules molecular monomers mRNA nitrogenous bases normal nucleic acids nucleotides organic pairs particular pentose phosphate group polymers polynucleotide polynucleotide strand polypeptide chain primary structure production properties Protein Structure purines pyrimidine result ribosomes ring secondary separated sequence of bases serve shape share shown sickle-cell disease similar specific starch Steroids strand sugar sugar-phosphate backbone synthesis three-dimensional types unique
Bibliographic information
| Title | Biology, Pages 82-91 Biology, Neil A. Campbell |
| Author | Neil A. Campbell |
| Edition | 7 |
| Publisher | Pearson, Benjamin Cummings, 2005 |
| Original from | the University of California |
| Digitized | 29 Jul 2011 |
| Length | 1231 pages |
| Export Citation | BiBTeX EndNote RefMan |